NUCLEOTIDE-SEQUENCE OF CDNA AND DERIVED AMINO-ACID-SEQUENCE OF HUMAN-COMPLEMENT COMPONENT-C9
NUCLEOTIDE-SEQUENCE OF CDNA AND DERIVED AMINO-ACID-SEQUENCE OF HUMAN-COMPLEMENT COMPONENT-C9
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DOI：
10.1073/pnas.81.23.7298
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发表时间：
1984-01-01
期刊：
影响因子：
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通讯作者：
FEY, GH
中科院分区：
文献类型：
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作者：
DISCIPIO, RG;GEHRING, MR;FEY, GH
测定了编码人补体第九组分（C9）的核苷酸序列，并推导出相应的氨基酸序列。通过菌落杂交技术，使用2种对应于C9氨基酸序列已知区域的放射性标记寡核苷酸探针，筛选人肝cDNA [互补DNA]文库。分离了两个重组质粒，并对其cDNA插入片段进行了测序。衍生的蛋白质序列由单个多肽链中的537个氨基酸组成。亲水指数与序列号的关系曲线表明，C9的氨基末端的一半主要是亲水性的，而该蛋白质的羧基末端部分更疏水。C9的一级结构的两亲性组织与聚合的C9穿透脂质双层的已知潜力一致，从而导致跨膜通道的形成。
The nucleotide sequence coding for the ninth component of human complement (C9) was determined and the corresponding amino acid sequence was derived. A human liver cDNA [complementary DNA] library was screened by the colony-hybridization technique using 2 radiolabeled oligonucleotide probes that correspond to known regions of the C9 amino acid sequence. Two recombinant plasmids were isolated and their cDNA inserts were sequenced. The derived protein sequence consists of 537 amino acids in a single polypeptide chain. A profile of the hydropathic index vs. sequence number indicates that the amino-terminal half of the C9 is predominantly hydrophilic in character whereas the carboxyl-terminal section of this protein is more hydrophobic. The amphipathic organization of the primary structure of C9 is consistent with the known potential of polymerized C9 to penetrate lipid bilayers, causing the formation of transmembrane channels.